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SURE_PSEPK
ID   SURE_PSEPK              Reviewed;         249 AA.
AC   Q88MF1;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=5'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060};
DE   AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060};
GN   Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; OrderedLocusNames=PP_1620;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside
CC       5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00060};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   -!- SIMILARITY: Belongs to the SurE nucleotidase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00060}.
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DR   EMBL; AE015451; AAN67241.1; -; Genomic_DNA.
DR   RefSeq; NP_743777.1; NC_002947.4.
DR   RefSeq; WP_010952690.1; NC_002947.4.
DR   AlphaFoldDB; Q88MF1; -.
DR   SMR; Q88MF1; -.
DR   STRING; 160488.PP_1620; -.
DR   EnsemblBacteria; AAN67241; AAN67241; PP_1620.
DR   KEGG; ppu:PP_1620; -.
DR   PATRIC; fig|160488.4.peg.1711; -.
DR   eggNOG; COG0496; Bacteria.
DR   HOGENOM; CLU_045192_1_2_6; -.
DR   OMA; DCVHIAL; -.
DR   PhylomeDB; Q88MF1; -.
DR   BioCyc; PPUT160488:G1G01-1717-MON; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1210.10; -; 1.
DR   HAMAP; MF_00060; SurE; 1.
DR   InterPro; IPR030048; SurE.
DR   InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR   InterPro; IPR036523; SurE-like_sf.
DR   PANTHER; PTHR30457; PTHR30457; 1.
DR   Pfam; PF01975; SurE; 1.
DR   SUPFAM; SSF64167; SSF64167; 1.
DR   TIGRFAMs; TIGR00087; surE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..249
FT                   /note="5'-nucleotidase SurE"
FT                   /id="PRO_0000111832"
FT   BINDING         8
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         9
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         39
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         91
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
SQ   SEQUENCE   249 AA;  26317 MW;  824F1D5E7CFB8073 CRC64;
     MRILISNDDG VTAPGIAALH AALADYAECA VIAPDQDKSG ASSSLTLDRP LHPQTLANGF
     ISLNGTPTDC VHLGLNGLLP QMPDMVVSGI NLGANLGDDV LYSGTVAAAL EGRFLGGTSL
     AFSLLSRQPD NLPTAAYIAR RLVEAQSRLV LPPRTVLNVN IPNLPLEHIR GIQLTRLGHR
     ARAAAPTKVV NPRGKEGYWI AVAGDAEDGG PGTDFHAVMQ GYVSITPLQL DRTFNDAFEQ
     LDGWLEGLL
 
 
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